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Conserved domains on  [gi|1998592409|ref|WP_206607095|]
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MULTISPECIES: MarR family winged helix-turn-helix transcriptional regulator [Sandaracinus]

Protein Classification

MarR family winged helix-turn-helix transcriptional regulator( domain architecture ID 11448790)

MarR family winged helix-turn-helix (wHTH) transcriptional regulator similar to Bacillus thuringiensis DNA-binding transcriptional repressor TubR, a DNA-binding protein that is part of the type III plasmid partition system used to ensure correct segregation of the pBtoxis plasmid

Gene Ontology:  GO:0006355|GO:0003700
PubMed:  10498949|28670937
SCOP:  4000246

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
3-140 3.85e-13

DNA-binding transcriptional regulator, MarR family [Transcription];


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 62.29  E-value: 3.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998592409   3 ERDAVRRIQVAYPKIWHACHRHPSAAARGGGLTERQGTVLVHLADGALSRPADLARHLGIAPSTLSEAIDQLVERGMVER 82
Cdd:COG1846     5 PDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVER 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1998592409  83 RRHTDDRRRTDFEVTEVGHRAVEEGSPLDPARLRAALAWLSAEERARAVEGLTLLADA 140
Cdd:COG1846    85 EPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAEN 142
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
3-140 3.85e-13

DNA-binding transcriptional regulator, MarR family [Transcription];


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 62.29  E-value: 3.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998592409   3 ERDAVRRIQVAYPKIWHACHRHPSAAARGGGLTERQGTVLVHLADGALSRPADLARHLGIAPSTLSEAIDQLVERGMVER 82
Cdd:COG1846     5 PDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVER 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1998592409  83 RRHTDDRRRTDFEVTEVGHRAVEEGSPLDPARLRAALAWLSAEERARAVEGLTLLADA 140
Cdd:COG1846    85 EPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAEN 142
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 33-81 3.29e-07

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 44.89  E-value: 3.29e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1998592409  33 GLTERQGTVLVHLADGALSRPADLARHLGIAPSTLSEAIDQLVERGMVE 81
Cdd:pfam12802   2 GLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVE 50
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
33-127 5.16e-06

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 42.58  E-value: 5.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998592409   33 GLTERQGTVLVHLAD-GALSrPADLARHLGIAPSTLSEAIDQLVERGMVERRRHTDDRRRTDFEVTEVGHRAVEEGSPLD 111
Cdd:smart00347   7 GLTPTQFLVLRILYEeGPLS-VSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEAR 85

                           90
                   ....*....|....*.
gi 1998592409  112 PARLRAALAWLSAEER 127
Cdd:smart00347  86 SETLAELLAGLTAEEQ 101
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 41-81 2.08e-03

Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.


Pssm-ID: 238042 [Multi-domain]  Cd Length: 78  Bit Score: 34.97  E-value: 2.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1998592409  41 VLVHLADGALSrPADLARHLGIAPSTLSEAIDQLVERGMVE 81
Cdd:cd00090    12 ILRLLLEGPLT-VSELAERLGLSQSTVSRHLKKLEEAGLVE 51
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
34-122 2.57e-03

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 37.12  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998592409  34 LTERQGTVLVHLADGALSRPADLARHLGIAPSTLSEAIDQLVERGMVERRRHTDDRrrtdFEVTEVGHRAVEEGSP---- 109
Cdd:PRK04172    4 LHPNEKKVLKALKELKEATLEELAEKLGLPPEAVMRAAEWLEEKGLVKVEERVEEV----YVLTEEGKKYAEEGLPerrl 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1998592409 110 -------------------LDPARLRAALAWL 122
Cdd:PRK04172   80 lnalkdggevsldelkealLDKKEVGIALGNL 111
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
3-140 3.85e-13

DNA-binding transcriptional regulator, MarR family [Transcription];


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 62.29  E-value: 3.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998592409   3 ERDAVRRIQVAYPKIWHACHRHPSAAARGGGLTERQGTVLVHLADGALSRPADLARHLGIAPSTLSEAIDQLVERGMVER 82
Cdd:COG1846     5 PDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVER 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1998592409  83 RRHTDDRRRTDFEVTEVGHRAVEEGSPLDPARLRAALAWLSAEERARAVEGLTLLADA 140
Cdd:COG1846    85 EPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAEN 142
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 33-81 3.29e-07

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 44.89  E-value: 3.29e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1998592409  33 GLTERQGTVLVHLADGALSRPADLARHLGIAPSTLSEAIDQLVERGMVE 81
Cdd:pfam12802   2 GLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVE 50
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
33-127 5.16e-06

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 42.58  E-value: 5.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998592409   33 GLTERQGTVLVHLAD-GALSrPADLARHLGIAPSTLSEAIDQLVERGMVERRRHTDDRRRTDFEVTEVGHRAVEEGSPLD 111
Cdd:smart00347   7 GLTPTQFLVLRILYEeGPLS-VSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEAR 85

                           90
                   ....*....|....*.
gi 1998592409  112 PARLRAALAWLSAEER 127
Cdd:smart00347  86 SETLAELLAGLTAEEQ 101
COG3398 COG3398
Predicted transcriptional regulator, contains two HTH domains [Transcription];
38-81 2.15e-05

Predicted transcriptional regulator, contains two HTH domains [Transcription];


Pssm-ID: 442625 [Multi-domain]  Cd Length: 159  Bit Score: 42.17  E-value: 2.15e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1998592409  38 QGTVLVHLADGALSRPADLARHLGIAPSTLSEAIDQLVERGMVE 81
Cdd:COG3398    99 PRRILLYLLENPGATNKELAEELGISRSTVSWHLKRLEEDGLVE 142
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
34-81 2.49e-04

Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 38.65  E-value: 2.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1998592409  34 LTERQGTVlvhladgalsRPADLARHLGIAPSTLSEAIDQLVERGMVE 81
Cdd:COG1321    18 LSEEGGPV----------RTSDIAERLGVSPPSVTEMLKKLEEKGLVE 55
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 34-85 1.04e-03

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 426012 [Multi-domain]  Cd Length: 59  Bit Score: 35.60  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1998592409  34 LTERQGTVLVHLAD-GALSrPADLARHLGIAPSTLSEAIDQLVERGMVERRRH 85
Cdd:pfam01047   1 LTLTQFHILRILYEhGPLT-VSELAEKLGVSKSTVTRVLDRLEKKGLIERSRS 52
HTH_ARSR smart00418
helix_turn_helix, Arsenical Resistance Operon Repressor;
41-81 1.86e-03

helix_turn_helix, Arsenical Resistance Operon Repressor;


Pssm-ID: 197713 [Multi-domain]  Cd Length: 66  Bit Score: 34.88  E-value: 1.86e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1998592409   41 VLVHLADGALSrPADLARHLGIAPSTLSEAIDQLVERGMVE 81
Cdd:smart00418   2 ILKLLAEGELC-VCELAEILGLSQSTVSHHLKKLREAGLVE 41
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 41-81 2.08e-03

Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.


Pssm-ID: 238042 [Multi-domain]  Cd Length: 78  Bit Score: 34.97  E-value: 2.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1998592409  41 VLVHLADGALSrPADLARHLGIAPSTLSEAIDQLVERGMVE 81
Cdd:cd00090    12 ILRLLLEGPLT-VSELAERLGLSQSTVSRHLKKLEEAGLVE 51
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
34-122 2.57e-03

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 37.12  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998592409  34 LTERQGTVLVHLADGALSRPADLARHLGIAPSTLSEAIDQLVERGMVERRRHTDDRrrtdFEVTEVGHRAVEEGSP---- 109
Cdd:PRK04172    4 LHPNEKKVLKALKELKEATLEELAEKLGLPPEAVMRAAEWLEEKGLVKVEERVEEV----YVLTEEGKKYAEEGLPerrl 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1998592409 110 -------------------LDPARLRAALAWL 122
Cdd:PRK04172   80 lnalkdggevsldelkealLDKKEVGIALGNL 111
COG4742 COG4742
Predicted transcriptional regulator, contains HTH domain [Transcription];
41-110 5.06e-03

Predicted transcriptional regulator, contains HTH domain [Transcription];


Pssm-ID: 443776 [Multi-domain]  Cd Length: 267  Bit Score: 36.03  E-value: 5.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998592409  41 VLVHLADGALSRpADLARHLGIAPSTLSEAIDQLVERGMVErrrhtddRRRTDFEVTEVGHRAVEEGSPL 110
Cdd:COG4742    21 ILLLLAEGPKTR-SELAESLDVSRSTILRQLKELEERGLIE-------RDDGEYELTTLGRLVVEEMEPL 82
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
 55-81 5.25e-03

Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.


Pssm-ID: 153418 [Multi-domain]  Cd Length: 66  Bit Score: 33.57  E-value: 5.25e-03
                          10        20
                  ....*....|....*....|....*..
gi 1998592409  55 DLARHLGIAPSTLSEAIDQLVERGMVE 81
Cdd:cd07377    30 ELAEELGVSRTTVREALRELEAEGLVE 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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